ID   ERG24_MOUSE             Reviewed;         418 AA.
AC   Q71KT5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-MAR-2009, entry version 34.
DE   RecName: Full=Delta(14)-sterol reductase;
DE            Short=Delta-14-SR;
DE            EC=1.3.1.70;
DE   AltName: Full=C-14 sterol reductase;
DE   AltName: Full=Sterol C14-reductase;
DE   AltName: Full=Transmembrane 7 superfamily member 2;
GN   Name=Tm7sf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Roberti R., Bennati A.M.;
RT   "cDNA cloning and expression of the gene encoding the mouse C-14
RT   sterol reductase.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Involved in the conversion of lanosterol to cholesterol.
CC   -!- CATALYTIC ACTIVITY: 4,4-dimethyl-5-alpha-cholesta-8,24-dien-3-
CC       beta-ol + NADP(+) = 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3-
CC       beta-ol + NADPH.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the ERG4/ERG24 family.
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DR   EMBL; AF480070; AAQ05836.1; -; mRNA.
DR   EMBL; AK155475; BAE33285.1; -; mRNA.
DR   IPI; IPI00751362; -.
DR   UniGene; Mm.458077; -.
DR   Ensembl; ENSMUSG00000024799; Mus musculus.
DR   MGI; MGI:1920416; Tm7sf2.
DR   HOGENOM; Q71KT5; -.
DR   HOVERGEN; Q71KT5; -.
DR   Bgee; Q71KT5; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050613; F:delta14-sterol reductase activity; IEA:EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001171; Ergosterol_biosynth_ERG4_ERG24.
DR   InterPro; IPR018083; Sterol_reductase_CS.
DR   Pfam; PF01222; ERG4_ERG24; 1.
DR   PROSITE; PS01017; STEROL_REDUCT_1; 1.
DR   PROSITE; PS01018; STEROL_REDUCT_2; 1.
PE   2: Evidence at transcript level;
KW   Cholesterol biosynthesis; Endoplasmic reticulum; Lipid synthesis;
KW   Membrane; NADP; Oxidoreductase; Steroid biosynthesis;
KW   Sterol biosynthesis; Transmembrane.
FT   CHAIN         1    418       Delta(14)-sterol reductase.
FT                                /FTId=PRO_0000331121.
FT   TRANSMEM     13     35       Potential.
FT   TRANSMEM     62     81       Potential.
FT   TRANSMEM    102    124       Potential.
FT   TRANSMEM    129    148       Potential.
FT   TRANSMEM    255    277       Potential.
FT   TRANSMEM    287    304       Potential.
FT   TRANSMEM    355    377       Potential.
SQ   SEQUENCE   418 AA;  46493 MW;  05DCB3E4B9422D31 CRC64;
     MTSREASQAP LEFGGPLGVA ALLILLPATM FHLLLAARSG PARLLALPAY LPGLEELWSP
     WALLLLFIWL GLQVALYLLP ARKVAEGLEL KDKSRLRYPI NGFQALVLTA LLMGLGVSVG
     LPLGALPGML LPLAFATTLT SFIFSLLLYA KALVAPASAL APGGNSGNSM YDFFLGRELN
     PRLGSFDFKY FCELRPGLIG WVFINLALLM QEAELRGSPS LAMWLVNGFQ LLYVGDALWY
     EESVLTTMDI IHDGFGFMLV FGDLAWVPFT YSLQAQFLLY HPQPLGLPMA LLICLLKAIG
     YYIFRGANSQ KNTFRKNPSD PSVAGLETIP TATGRQLLVS GWWGMVRHPN YLGDLIMALA
     WSLPCGLSHL LPYFYVLYFT ALLVHREARD EQQCLQKYGR AWQEYCKRVP YRIIPYVY
//